Sortilin, neurotensin receptor 3,; Sortilin, also known in mammals as neurotensin receptor-3, ...
92-286
3.52e-16
Sortilin, neurotensin receptor 3,; Sortilin, also known in mammals as neurotensin receptor-3, is the archetypical member of a Vps10-domain (Vps10-D) that binds neurotrophic factors and neuropeptides. This domain constitutes the entire luminal part of Sortilin and is activated in the trans-Golgi network by enzymatic propeptide cleavage. The structure of the domain has been determined as a ten-bladed propeller, with up to 9 BNR or beta-hairpin turns in it. The mature receptor binds various ligands, including its own propeptide (Sort-pro), neurotensin, the pro-forms of nerve growth factor-beta (NGF)6 and brain-derived neurotrophic factor (BDNF)7, lipoprotein lipase (LpL), apo lipoprotein AV14 and the receptor-associated protein (RAP)1.
Pssm-ID: 464929 [Multi-domain] Cd Length: 444 Bit Score: 82.25 E-value: 3.52e-16
Sortilin, neurotensin receptor 3,; Sortilin, also known in mammals as neurotensin receptor-3, ...
604-715
3.56e-08
Sortilin, neurotensin receptor 3,; Sortilin, also known in mammals as neurotensin receptor-3, is the archetypical member of a Vps10-domain (Vps10-D) that binds neurotrophic factors and neuropeptides. This domain constitutes the entire luminal part of Sortilin and is activated in the trans-Golgi network by enzymatic propeptide cleavage. The structure of the domain has been determined as a ten-bladed propeller, with up to 9 BNR or beta-hairpin turns in it. The mature receptor binds various ligands, including its own propeptide (Sort-pro), neurotensin, the pro-forms of nerve growth factor-beta (NGF)6 and brain-derived neurotrophic factor (BDNF)7, lipoprotein lipase (LpL), apo lipoprotein AV14 and the receptor-associated protein (RAP)1.
Pssm-ID: 464929 [Multi-domain] Cd Length: 444 Bit Score: 57.21 E-value: 3.56e-08
Non-viral sialidases; Sialidases or neuraminidases function to bind and hydrolyze terminal ...
94-315
8.40e-06
Non-viral sialidases; Sialidases or neuraminidases function to bind and hydrolyze terminal sialic acid residues from various glycoconjugates, they play vital roles in pathogenesis, bacterial nutrition and cellular interactions. They have a six-bladed, beta-propeller fold with the non-viral sialidases containing 2-5 Asp-box motifs (most commonly Ser/Thr-X-Asp-[X]-Gly-X-Thr- Trp/Phe). This CD includes eubacterial and eukaryotic sialidases.
Pssm-ID: 271234 [Multi-domain] Cd Length: 339 Bit Score: 48.99 E-value: 8.40e-06
Sortilin, neurotensin receptor 3,; Sortilin, also known in mammals as neurotensin receptor-3, ...
253-363
2.92e-05
Sortilin, neurotensin receptor 3,; Sortilin, also known in mammals as neurotensin receptor-3, is the archetypical member of a Vps10-domain (Vps10-D) that binds neurotrophic factors and neuropeptides. This domain constitutes the entire luminal part of Sortilin and is activated in the trans-Golgi network by enzymatic propeptide cleavage. The structure of the domain has been determined as a ten-bladed propeller, with up to 9 BNR or beta-hairpin turns in it. The mature receptor binds various ligands, including its own propeptide (Sort-pro), neurotensin, the pro-forms of nerve growth factor-beta (NGF)6 and brain-derived neurotrophic factor (BDNF)7, lipoprotein lipase (LpL), apo lipoprotein AV14 and the receptor-associated protein (RAP)1.
Pssm-ID: 464929 [Multi-domain] Cd Length: 444 Bit Score: 47.97 E-value: 2.92e-05
Non-viral sialidases; Sialidases or neuraminidases function to bind and hydrolyze terminal ...
199-403
3.11e-05
Non-viral sialidases; Sialidases or neuraminidases function to bind and hydrolyze terminal sialic acid residues from various glycoconjugates, they play vital roles in pathogenesis, bacterial nutrition and cellular interactions. They have a six-bladed, beta-propeller fold with the non-viral sialidases containing 2-5 Asp-box motifs (most commonly Ser/Thr-X-Asp-[X]-Gly-X-Thr- Trp/Phe). This CD includes eubacterial and eukaryotic sialidases.
Pssm-ID: 271234 [Multi-domain] Cd Length: 339 Bit Score: 47.45 E-value: 3.11e-05
Non-viral sialidases; Sialidases or neuraminidases function to bind and hydrolyze terminal ...
540-745
2.17e-03
Non-viral sialidases; Sialidases or neuraminidases function to bind and hydrolyze terminal sialic acid residues from various glycoconjugates, they play vital roles in pathogenesis, bacterial nutrition and cellular interactions. They have a six-bladed, beta-propeller fold with the non-viral sialidases containing 2-5 Asp-box motifs (most commonly Ser/Thr-X-Asp-[X]-Gly-X-Thr- Trp/Phe). This CD includes eubacterial and eukaryotic sialidases.
Pssm-ID: 271234 [Multi-domain] Cd Length: 339 Bit Score: 41.67 E-value: 2.17e-03
Sortilin, neurotensin receptor 3,; Sortilin, also known in mammals as neurotensin receptor-3, ...
92-286
3.52e-16
Sortilin, neurotensin receptor 3,; Sortilin, also known in mammals as neurotensin receptor-3, is the archetypical member of a Vps10-domain (Vps10-D) that binds neurotrophic factors and neuropeptides. This domain constitutes the entire luminal part of Sortilin and is activated in the trans-Golgi network by enzymatic propeptide cleavage. The structure of the domain has been determined as a ten-bladed propeller, with up to 9 BNR or beta-hairpin turns in it. The mature receptor binds various ligands, including its own propeptide (Sort-pro), neurotensin, the pro-forms of nerve growth factor-beta (NGF)6 and brain-derived neurotrophic factor (BDNF)7, lipoprotein lipase (LpL), apo lipoprotein AV14 and the receptor-associated protein (RAP)1.
Pssm-ID: 464929 [Multi-domain] Cd Length: 444 Bit Score: 82.25 E-value: 3.52e-16
Sortilin, neurotensin receptor 3,; Sortilin, also known in mammals as neurotensin receptor-3, ...
604-715
3.56e-08
Sortilin, neurotensin receptor 3,; Sortilin, also known in mammals as neurotensin receptor-3, is the archetypical member of a Vps10-domain (Vps10-D) that binds neurotrophic factors and neuropeptides. This domain constitutes the entire luminal part of Sortilin and is activated in the trans-Golgi network by enzymatic propeptide cleavage. The structure of the domain has been determined as a ten-bladed propeller, with up to 9 BNR or beta-hairpin turns in it. The mature receptor binds various ligands, including its own propeptide (Sort-pro), neurotensin, the pro-forms of nerve growth factor-beta (NGF)6 and brain-derived neurotrophic factor (BDNF)7, lipoprotein lipase (LpL), apo lipoprotein AV14 and the receptor-associated protein (RAP)1.
Pssm-ID: 464929 [Multi-domain] Cd Length: 444 Bit Score: 57.21 E-value: 3.56e-08
Sortilin, neurotensin receptor 3,; Sortilin, also known in mammals as neurotensin receptor-3, ...
535-674
3.94e-06
Sortilin, neurotensin receptor 3,; Sortilin, also known in mammals as neurotensin receptor-3, is the archetypical member of a Vps10-domain (Vps10-D) that binds neurotrophic factors and neuropeptides. This domain constitutes the entire luminal part of Sortilin and is activated in the trans-Golgi network by enzymatic propeptide cleavage. The structure of the domain has been determined as a ten-bladed propeller, with up to 9 BNR or beta-hairpin turns in it. The mature receptor binds various ligands, including its own propeptide (Sort-pro), neurotensin, the pro-forms of nerve growth factor-beta (NGF)6 and brain-derived neurotrophic factor (BDNF)7, lipoprotein lipase (LpL), apo lipoprotein AV14 and the receptor-associated protein (RAP)1.
Pssm-ID: 464929 [Multi-domain] Cd Length: 444 Bit Score: 50.66 E-value: 3.94e-06
Non-viral sialidases; Sialidases or neuraminidases function to bind and hydrolyze terminal ...
94-315
8.40e-06
Non-viral sialidases; Sialidases or neuraminidases function to bind and hydrolyze terminal sialic acid residues from various glycoconjugates, they play vital roles in pathogenesis, bacterial nutrition and cellular interactions. They have a six-bladed, beta-propeller fold with the non-viral sialidases containing 2-5 Asp-box motifs (most commonly Ser/Thr-X-Asp-[X]-Gly-X-Thr- Trp/Phe). This CD includes eubacterial and eukaryotic sialidases.
Pssm-ID: 271234 [Multi-domain] Cd Length: 339 Bit Score: 48.99 E-value: 8.40e-06
Sortilin, neurotensin receptor 3,; Sortilin, also known in mammals as neurotensin receptor-3, ...
253-363
2.92e-05
Sortilin, neurotensin receptor 3,; Sortilin, also known in mammals as neurotensin receptor-3, is the archetypical member of a Vps10-domain (Vps10-D) that binds neurotrophic factors and neuropeptides. This domain constitutes the entire luminal part of Sortilin and is activated in the trans-Golgi network by enzymatic propeptide cleavage. The structure of the domain has been determined as a ten-bladed propeller, with up to 9 BNR or beta-hairpin turns in it. The mature receptor binds various ligands, including its own propeptide (Sort-pro), neurotensin, the pro-forms of nerve growth factor-beta (NGF)6 and brain-derived neurotrophic factor (BDNF)7, lipoprotein lipase (LpL), apo lipoprotein AV14 and the receptor-associated protein (RAP)1.
Pssm-ID: 464929 [Multi-domain] Cd Length: 444 Bit Score: 47.97 E-value: 2.92e-05
Non-viral sialidases; Sialidases or neuraminidases function to bind and hydrolyze terminal ...
199-403
3.11e-05
Non-viral sialidases; Sialidases or neuraminidases function to bind and hydrolyze terminal sialic acid residues from various glycoconjugates, they play vital roles in pathogenesis, bacterial nutrition and cellular interactions. They have a six-bladed, beta-propeller fold with the non-viral sialidases containing 2-5 Asp-box motifs (most commonly Ser/Thr-X-Asp-[X]-Gly-X-Thr- Trp/Phe). This CD includes eubacterial and eukaryotic sialidases.
Pssm-ID: 271234 [Multi-domain] Cd Length: 339 Bit Score: 47.45 E-value: 3.11e-05
Sortilin, neurotensin receptor 3,; Sortilin, also known in mammals as neurotensin receptor-3, ...
657-719
6.20e-05
Sortilin, neurotensin receptor 3,; Sortilin, also known in mammals as neurotensin receptor-3, is the archetypical member of a Vps10-domain (Vps10-D) that binds neurotrophic factors and neuropeptides. This domain constitutes the entire luminal part of Sortilin and is activated in the trans-Golgi network by enzymatic propeptide cleavage. The structure of the domain has been determined as a ten-bladed propeller, with up to 9 BNR or beta-hairpin turns in it. The mature receptor binds various ligands, including its own propeptide (Sort-pro), neurotensin, the pro-forms of nerve growth factor-beta (NGF)6 and brain-derived neurotrophic factor (BDNF)7, lipoprotein lipase (LpL), apo lipoprotein AV14 and the receptor-associated protein (RAP)1.
Pssm-ID: 464929 [Multi-domain] Cd Length: 444 Bit Score: 46.81 E-value: 6.20e-05
Sortilin, neurotensin receptor 3,; Sortilin, also known in mammals as neurotensin receptor-3, ...
305-404
7.89e-05
Sortilin, neurotensin receptor 3,; Sortilin, also known in mammals as neurotensin receptor-3, is the archetypical member of a Vps10-domain (Vps10-D) that binds neurotrophic factors and neuropeptides. This domain constitutes the entire luminal part of Sortilin and is activated in the trans-Golgi network by enzymatic propeptide cleavage. The structure of the domain has been determined as a ten-bladed propeller, with up to 9 BNR or beta-hairpin turns in it. The mature receptor binds various ligands, including its own propeptide (Sort-pro), neurotensin, the pro-forms of nerve growth factor-beta (NGF)6 and brain-derived neurotrophic factor (BDNF)7, lipoprotein lipase (LpL), apo lipoprotein AV14 and the receptor-associated protein (RAP)1.
Pssm-ID: 464929 [Multi-domain] Cd Length: 444 Bit Score: 46.42 E-value: 7.89e-05
Photosynthesis system II assembly factor YCF48; YCF48 is one of several assembly factors of ...
95-390
1.11e-04
Photosynthesis system II assembly factor YCF48; YCF48 is one of several assembly factors of the photosynthesis system II. The photosynthesis system II occurs in Cyanobacteria that are Gram-negative bacteria performing oxygenic photosynthesis. One of the three membranes surrounding these bacteria is the inner thylakoid membrane (TM) system that is localized within the cell and houses the large pigment-protein complexes of the photosynthetic electron transfer chain, i.e. Photosystem (PS) II, PSI, the cytochrome b6f complex, and the ATP synthase. YCF48 is necessary for efficient assembly and repair of the PSII. YCF48 is found predominantly in the thykaloid membrane. It is a BNR repeat protein.
Pssm-ID: 405545 [Multi-domain] Cd Length: 304 Bit Score: 45.38 E-value: 1.11e-04
Non-viral sialidases; Sialidases or neuraminidases function to bind and hydrolyze terminal ...
73-267
4.27e-04
Non-viral sialidases; Sialidases or neuraminidases function to bind and hydrolyze terminal sialic acid residues from various glycoconjugates, they play vital roles in pathogenesis, bacterial nutrition and cellular interactions. They have a six-bladed, beta-propeller fold with the non-viral sialidases containing 2-5 Asp-box motifs (most commonly Ser/Thr-X-Asp-[X]-Gly-X-Thr- Trp/Phe). This CD includes eubacterial and eukaryotic sialidases.
Pssm-ID: 271234 [Multi-domain] Cd Length: 339 Bit Score: 43.60 E-value: 4.27e-04
Non-viral sialidases; Sialidases or neuraminidases function to bind and hydrolyze terminal ...
86-228
1.50e-03
Non-viral sialidases; Sialidases or neuraminidases function to bind and hydrolyze terminal sialic acid residues from various glycoconjugates, they play vital roles in pathogenesis, bacterial nutrition and cellular interactions. They have a six-bladed, beta-propeller fold with the non-viral sialidases containing 2-5 Asp-box motifs (most commonly Ser/Thr-X-Asp-[X]-Gly-X-Thr- Trp/Phe). This CD includes eubacterial and eukaryotic sialidases.
Pssm-ID: 271234 [Multi-domain] Cd Length: 339 Bit Score: 42.06 E-value: 1.50e-03
Non-viral sialidases; Sialidases or neuraminidases function to bind and hydrolyze terminal ...
540-745
2.17e-03
Non-viral sialidases; Sialidases or neuraminidases function to bind and hydrolyze terminal sialic acid residues from various glycoconjugates, they play vital roles in pathogenesis, bacterial nutrition and cellular interactions. They have a six-bladed, beta-propeller fold with the non-viral sialidases containing 2-5 Asp-box motifs (most commonly Ser/Thr-X-Asp-[X]-Gly-X-Thr- Trp/Phe). This CD includes eubacterial and eukaryotic sialidases.
Pssm-ID: 271234 [Multi-domain] Cd Length: 339 Bit Score: 41.67 E-value: 2.17e-03
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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Functional characterization of the conserved domain architecture found on the query.
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This image shows a graphical summary of conserved domains identified on the query sequence.
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if a domain or superfamily has been annotated with functional sites (conserved features),
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click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.
The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
Click on the domain model's accession number to view the multiple sequence alignment of the proteins used to develop the corresponding domain model.
To view your query sequence embedded in that multiple sequence alignment, click on the colored bars in the Graphical Summary portion of the search results page,
or click on the triangles, if present, that represent functional sites (conserved features)
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Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence.
(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
(labeled illustration) Full Display shows all domain models, in each hit category below, that meet or exceed the RPS-BLAST threshold for statistical significance.
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and represent a very high confidence that the query sequence belongs to the same protein family as the sequences use to create the domain model
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Retrieve proteins that contain one or more of the domains present in the query sequence, using the Conserved Domain Architecture Retrieval Tool
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